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Conserved domains on  [gi|371560576|gb|AEX37068|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Sphingobium sp. 031]

Protein Classification

type I glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 1903262)

type I glyceraldehyde-3-phosphate dehydrogenase catalyzes the NAD-dependent oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GapA super family cl43010
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-145 5.92e-99

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


The actual alignment was detected with superfamily member COG0057:

Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 287.29  E-value: 5.92e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:COG0057  164 LNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVD 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:COG0057  244 LTVELEKETTVEEVNAALKEAAE-GPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLV 307
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-145 5.92e-99

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 287.29  E-value: 5.92e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:COG0057  164 LNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVD 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:COG0057  244 LTVELEKETTVEEVNAALKEAAE-GPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLV 307
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-145 2.94e-89

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 256.61  E-value: 2.94e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:cd18126   13 LNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:cd18126   93 LTVRLEKPVTVEEVNAALKKAAE-GPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLV 156
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-145 1.62e-72

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 213.99  E-value: 1.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576    1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHS-DMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVV 79
Cdd:pfam02800   8 LNDNFGIKKGLMTTVHAYTNDQKLLDGPHHkDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 371560576   80 DLKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:pfam02800  88 DLVVELEKPVTVEEVNAALKEAAE-GALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFV 152
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-142 1.04e-71

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 217.92  E-value: 1.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576    1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:TIGR01534 163 LDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVD 242

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 371560576   81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDG 142
Cdd:TIGR01534 243 LVVNLEKDVTVEEVNAALKEASE-GELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGL 303
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-145 1.74e-66

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 204.97  E-value: 1.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:PRK07729 164 LDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVD 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:PRK07729 244 LVVDVKRDVTVEEINEAFKTAAN-GALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKV 307
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-145 5.92e-99

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 287.29  E-value: 5.92e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:COG0057  164 LNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVD 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:COG0057  244 LTVELEKETTVEEVNAALKEAAE-GPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLV 307
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-145 2.94e-89

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 256.61  E-value: 2.94e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:cd18126   13 LNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:cd18126   93 LTVRLEKPVTVEEVNAALKKAAE-GPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLV 156
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-145 1.62e-72

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 213.99  E-value: 1.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576    1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHS-DMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVV 79
Cdd:pfam02800   8 LNDNFGIKKGLMTTVHAYTNDQKLLDGPHHkDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 371560576   80 DLKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:pfam02800  88 DLVVELEKPVTVEEVNAALKEAAE-GALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFV 152
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-142 1.04e-71

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 217.92  E-value: 1.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576    1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:TIGR01534 163 LDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVD 242

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 371560576   81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDG 142
Cdd:TIGR01534 243 LVVNLEKDVTVEEVNAALKEASE-GELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGL 303
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-145 1.74e-66

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 204.97  E-value: 1.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:PRK07729 164 LDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVD 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:PRK07729 244 LVVDVKRDVTVEEINEAFKTAAN-GALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKV 307
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-145 4.82e-65

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 201.11  E-value: 4.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:PRK08955 164 IHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTD 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:PRK08955 244 CVFEVERDTTVEEVNALLKEAAE-GELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQV 307
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-145 1.03e-56

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 179.72  E-value: 1.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:PRK07403 166 LHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVD 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:PRK07403 246 LVVQVEKRTITEQVNEVLKDASE-GPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMV 309
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-145 1.29e-54

C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (E4PDH; EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467686  Cd Length: 165  Bit Score: 169.13  E-value: 1.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:cd23937   13 LDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIAVRVPTINVTAMD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:cd23937   93 LSVTLKKDVTAEEVNRVLRQASQ-GRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLV 156
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 1-143 9.16e-49

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 162.78  E-value: 9.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:PRK08289 301 VNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAI 380

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEAGPLKGVLGYSDEP-LVSIDYNGDPRSSTVDSLETaVVDGK 143
Cdd:PRK08289 381 LNLNLEKETSREELNEYLRQMSLHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQAT-IVNGN 443
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-145 1.78e-48

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 158.68  E-value: 1.78e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:PRK13535 166 LDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAID 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:PRK13535 246 LSVTVKKPVKVNEVNQLLQKAAQ-GAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLI 309
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-145 5.92e-48

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 158.94  E-value: 5.92e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:PLN03096 224 LDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVD 303

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  81 LKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:PLN03096 304 LVVQVEKKTFAEEVNAAFRDAAE-KELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMV 367
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-145 4.49e-47

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 157.75  E-value: 4.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLDQLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVD 80
Cdd:PLN02237 241 LDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVD 320

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 371560576  81 LKF-IPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:PLN02237 321 LVVnVEKKGITAEDVNAAFRKAAD-GPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMV 385
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 3-137 7.70e-44

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 147.51  E-value: 7.70e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   3 DAIGIESGFMTTIHSYTNDQNTLDQLH-SDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVDL 81
Cdd:PTZ00434 182 EGFGIETGLMTTIHSYTATQKTVDGVSvKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDL 261

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 371560576  82 KFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLET 137
Cdd:PTZ00434 262 TFRATRDTSIQEIDAAIKRASQ-TYMKGILGFTDDELVSADFINDNRSSIYDSKAT 316
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-134 1.42e-42

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 145.39  E-value: 1.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLD-QLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVV 79
Cdd:PLN02272 247 VHEEFGILEGLMTTVHATTATQKTVDgPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 326

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  80 DLKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDS 134
Cdd:PLN02272 327 DLTCRLEKSASYEDVKAAIKYASE-GPLKGILGYTDEDVVSNDFVGDSRSSIFDA 380
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-133 1.67e-37

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 130.34  E-value: 1.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLD---QLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVS 77
Cdd:PTZ00023 164 VNDKFGIVEGLMTTVHASTANQLTVDgpsKGGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVS 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 371560576  78 VVDLKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVD 133
Cdd:PTZ00023 244 VVDLTCKLAKPAKYEEIVAAVKKAAE-GPLKGILGYTDDEVVSSDFVHDKRSSIFD 298
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-134 8.89e-37

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 128.31  E-value: 8.89e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLD-QLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVV 79
Cdd:PRK15425 162 INDNFGIIEGLMTTVHATTATQKTVDgPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 241

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 371560576  80 DLKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDS 134
Cdd:PRK15425 242 DLTVRLEKAATYEQIKAAVKAAAE-GEMKGVLGYTEDDVVSTDFNGEVCTSVFDA 295
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 1-145 1.68e-36

C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467673  Cd Length: 164  Bit Score: 123.11  E-value: 1.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLD-QLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVV 79
Cdd:cd18123   13 IHDSFGIKKGRMTTVHAATDTQKTVDgPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGMAVRVPTTLMSVH 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 371560576  80 DLKFIPKRPTTKDEVNSLLKAASEAgplKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:cd18123   93 DLMVELEKDVTYDDIKEAVKQAPEG---KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEV 155
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-145 6.33e-35

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 123.68  E-value: 6.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLD-QLHSDMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVV 79
Cdd:PLN02358 168 INDRFGIVEGLMTTVHSITATQKTVDgPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVV 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 371560576  80 DLKFIPKRPTTKDEVNSLLKAASEaGPLKGVLGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:PLN02358 248 DLTVRLEKAATYDEIKKAIKEESE-GKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFV 312
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-145 1.64e-15

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 69.09  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576   1 LNDAIGIESGFMTTIHSYTNDQNTLD-QLHSDMrrARAAALSQIPTSTGAARAVGEVLPEL--KGKLDGSSIRVPTPNVS 77
Cdd:cd18122   13 LNDKFGIEEILVVTVQAVSGAGPKTKgPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIgkPIKVDGIAVRVPATLGH 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371560576  78 VVDLKFIPKRPTTKDEVNSLLKAASEAGPLKGVLGYSDEPlVSIDYNGDPRSSTVDSLETAVVDGKLV 145
Cdd:cd18122   91 LVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAK-VSTRSVGGVYGVPVGRQREFAFDDNKL 157
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 31-144 9.90e-12

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 61.04  E-value: 9.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560576  31 DMRRARAAALSQIPTSTGAARAVGEVLPELKGKLDGSSIRVPTPNVSVVDLKFIPKRPTTKDEVNSLLKAASeAGPLKGV 110
Cdd:PTZ00353 197 DWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAA-SDRLNGV 275

                         90       100       110
                 ....*....|....*....|....*....|....
gi 371560576 111 LGYSDEPLVSIDYNGDPRSSTVDSLETAVVDGKL 144
Cdd:PTZ00353 276 LCISKRDMISVDCIPNGKLCYDATSSSSSREGEV 309
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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